3ZM9

The mechanism of allosteric coupling in choline kinase a1 revealed by a rationally designed inhibitor

3ZM9 の概要

• エントリーDOI: 10.2210/pdb3zm9/pdb
• 分子名称: CHOLINE KINASE ALPHA, 1-(4-(4-(4-((6-amino-9H-purin-9-yl)methyl)phenyl)butyl)benzyl)-4- (dimethylamino)pyridinium (3 entities in total)
• 機能のキーワード: transferase, negative cooperativity, allosteric mechanism, elastic network analysis
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: P35790
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90894.19

構造登録者

Sahun-Roncero, M.,Rubio-Ruiz, B.,Saladino, G.,Conejo-Garcia, A.,Espinosa, A.,Velazquez-Campoy, A.,Gervasio, F.L.,Entrena, A.,Hurtado-Guerrero, R. (登録日: 2013-02-06, 公開日: 2013-02-27, 最終更新日: 2023-12-20)

主引用文献

Sahun-Roncero, M.,Rubio-Ruiz, B.,Saladino, G.,Conejo-Garcia, A.,Espinosa, A.,Velazquez-Campoy, A.,Gervasio, F.L.,Entrena, A.,Hurtado-Guerrero, R.
The Mechanism of Allosteric Coupling in Choline Kinase A1 Revealed by a Rationally Designed Inhibitor
Angew.Chem.Int.Ed.Engl., 52:4582-, 2013

PubMed Abstract: Applying a CHOK hold: Combined experimental and computational studies of the binding mode of a rationally designed inhibitor of the dimeric choline kinase α1 (CHOKα1) explain the molecular mechanism of negative cooperativity (see scheme) and how the monomers are connected. The results give insight into how the symmetry of the dimer can be partially conserved despite a lack of conservation in the static crystal structures.

PubMed: 23441033
DOI: 10.1002/ANIE.201209660

実験手法

X-RAY DIFFRACTION (1.9 Å)